Insights into the binding interaction of Reactive Yellow 145 with human serum albumin from a biophysics point of view

Farajzadeh-Dehkordi, Nazanin; Farhadian, Sadegh; Zahraei, Zohreh; Asgharzadeh, Sanaz; Shareghi, Behzad; Shakerian, Behnam

doi:10.1016/j.molliq.2022.120800

Journal of Molecular Liquids

2023

DOI: 10.1016/j.molliq.2022.120800

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Insights into the binding interaction of Reactive Yellow 145 with human serum albumin from a biophysics point of view

Nazanin Farajzadeh-Dehkordi

Sadegh Farhadian

Zohreh Zahraei

et al.

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Cited by 23 publications

References 56 publications

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Ligand-human serum albumin analysis: the near-UV CD and UV-Vis spectroscopic studies

Rogóż,

Owczarzy,

Kulig

et al. 2024

Naunyn-Schmiedeberg's Arch Pharmacol

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Spectroscopic methods offer many new opportunities to study protein–ligand interactions. The aim of this study was to evaluate the possibility of using near-UV CD as well as UV-Vis spectroscopic techniques to study the interaction between human serum albumin (HSA) and markers of Sudlow’s site I (warfarin, phenylbutazone) and II (ketoprofen, ibuprofen), as well as prednisolone and indapamide. In order to perform the planned measurements, near-UV CD spectropolarimetry and UV-Vis spectrophotometry have been used. It has been demonstrated that both techniques allow for rapid evaluation of non-covalent interactions between HSA and ligand, as well as identification of the HSA aromatic amino acid residues involved in this process. The near-UV CD spectroscopic data were more valuable than the analysis based on the second derivative of differential UV-Vis absorption spectra, especially for ligands with a non-specified binding site and low affinity towards HSA, such as prednisolone. The combination of both techniques makes it possible for comprehensive analysis of the interaction between HSA and ligands.

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Ligand-human serum albumin analysis: the near-UV CD and UV-Vis spectroscopic studies

Rogóż,

Owczarzy,

Kulig

et al. 2024

Naunyn-Schmiedeberg's Arch Pharmacol

View full text Add to dashboard Cite

show abstract

Characterization of caffeic acid-induced changes in the structure and stability of lysozyme: insights from spectroscopy and molecular dynamics simulations

Asemi-Esfahani,

Shareghi,

Farhadian

et al. 2023

J IRAN CHEM SOC

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Antioxidant properties of acteoside against biological systems: Hemoglobin and cardiomyocyte as potential models

Zhang,

Cui,

et al. 2024

Arabian Journal of Chemistry

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Insights into the binding interaction of Reactive Yellow 145 with human serum albumin from a biophysics point of view

Cited by 23 publications

References 56 publications

Ligand-human serum albumin analysis: the near-UV CD and UV-Vis spectroscopic studies

Ligand-human serum albumin analysis: the near-UV CD and UV-Vis spectroscopic studies

Characterization of caffeic acid-induced changes in the structure and stability of lysozyme: insights from spectroscopy and molecular dynamics simulations

Antioxidant properties of acteoside against biological systems: Hemoglobin and cardiomyocyte as potential models

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